MNAR1_HUMAN
ID MNAR1_HUMAN Reviewed; 916 AA.
AC Q9UPX6; A7MD43;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Major intrinsically disordered Notch2-binding receptor 1 {ECO:0000303|PubMed:29329397};
DE AltName: Full=Membrane integral NOTCH2-associated receptor 1;
DE AltName: Full=Ubiquitination and mTOR signaling protein {ECO:0000303|PubMed:30080879};
GN Name=MINAR1 {ECO:0000303|PubMed:29329397};
GN Synonyms=KIAA1024, UBTOR {ECO:0000303|PubMed:30080879};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND
RP INTERACTION WITH NOTCH2.
RX PubMed=29329397; DOI=10.1093/jmcb/mjy002;
RA Ho R.X., Meyer R.D., Chandler K.B., Ersoy E., Park M., Bondzie P.A.,
RA Rahimi N., Xu H., Costello C.E., Rahimi N.;
RT "MINAR1 is a Notch2-binding protein that inhibits angiogenesis and breast
RT cancer growth.";
RL J. Mol. Cell Biol. 10:195-204(2018).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH DEPTOR.
RX PubMed=30080879; DOI=10.1371/journal.pgen.1007583;
RA Zhang H., Zhang Q., Gao G., Wang X., Wang T., Kong Z., Wang G., Zhang C.,
RA Wang Y., Peng G.;
RT "UBTOR/KIAA1024 regulates neurite outgrowth and neoplasia through mTOR
RT signaling.";
RL PLoS Genet. 14:E1007583-E1007583(2018).
CC -!- FUNCTION: Intrinsically disordered protein which may negatively
CC regulate mTOR signaling pathway by stabilizing the mTOR complex
CC component DEPTOR (PubMed:30080879). Negatively regulates angiogenesis
CC (PubMed:29329397). Negatively regulates cell growth (PubMed:29329397,
CC PubMed:30080879). Negatively regulates neurite outgrowth in hippocampal
CC neurons (By similarity). {ECO:0000250|UniProtKB:D3ZJ47,
CC ECO:0000269|PubMed:29329397, ECO:0000269|PubMed:30080879}.
CC -!- SUBUNIT: Interacts with NOTCH2; this interaction increases MINAR1
CC stability (PubMed:29329397). Interacts (via N-terminus) with DEPTOR
CC (via PDZ domain); this interaction may stabilize DEPTOR protein by
CC impairing its ubiquitination (PubMed:30080879).
CC {ECO:0000269|PubMed:29329397, ECO:0000269|PubMed:30080879}.
CC -!- INTERACTION:
CC Q9UPX6; Q9Y5P4-2: CERT1; NbExp=3; IntAct=EBI-11977115, EBI-11156432;
CC Q9UPX6; Q9BW66: CINP; NbExp=3; IntAct=EBI-11977115, EBI-739784;
CC Q9UPX6; Q9BUL8: PDCD10; NbExp=3; IntAct=EBI-11977115, EBI-740195;
CC Q9UPX6; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-11977115, EBI-8652744;
CC Q9UPX6; Q15436: SEC23A; NbExp=3; IntAct=EBI-11977115, EBI-81088;
CC Q9UPX6; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-11977115, EBI-11994282;
CC Q9UPX6; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-11977115, EBI-765817;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29329397,
CC ECO:0000269|PubMed:30080879}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:30080879}.
CC -!- TISSUE SPECIFICITY: Widely expressed, including in breast epithelial
CC cells and endothelial cells (at protein level). Expression is down-
CC regulated in advanced breast tumors (at protein level).
CC {ECO:0000269|PubMed:29329397}.
CC -!- SIMILARITY: Belongs to the MINAR family. {ECO:0000305}.
CC -!- CAUTION: MINAR1 topology is a matter of debate, some authors think the
CC N-terminus is extracellular, while preliminary experimental results
CC suggest a cytosolic location. {ECO:0000305|PubMed:29329397,
CC ECO:0000305|PubMed:30080879}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82976.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB028947; BAA82976.2; ALT_INIT; mRNA.
DR EMBL; CH471136; EAW99137.1; -; Genomic_DNA.
DR EMBL; BC152466; AAI52467.1; -; mRNA.
DR CCDS; CCDS32306.1; -.
DR RefSeq; NP_056021.1; NM_015206.2.
DR RefSeq; XP_011519694.1; XM_011521392.1.
DR RefSeq; XP_011519695.1; XM_011521393.2.
DR RefSeq; XP_011519697.1; XM_011521395.2.
DR RefSeq; XP_011519698.1; XM_011521396.2.
DR RefSeq; XP_016877516.1; XM_017022027.1.
DR AlphaFoldDB; Q9UPX6; -.
DR BioGRID; 116855; 8.
DR IntAct; Q9UPX6; 7.
DR STRING; 9606.ENSP00000307461; -.
DR iPTMnet; Q9UPX6; -.
DR PhosphoSitePlus; Q9UPX6; -.
DR BioMuta; KIAA1024; -.
DR DMDM; 32699623; -.
DR EPD; Q9UPX6; -.
DR MassIVE; Q9UPX6; -.
DR PaxDb; Q9UPX6; -.
DR PeptideAtlas; Q9UPX6; -.
DR PRIDE; Q9UPX6; -.
DR ProteomicsDB; 85466; -.
DR Antibodypedia; 2612; 31 antibodies from 14 providers.
DR DNASU; 23251; -.
DR Ensembl; ENST00000305428.8; ENSP00000307461.3; ENSG00000169330.9.
DR GeneID; 23251; -.
DR KEGG; hsa:23251; -.
DR MANE-Select; ENST00000305428.8; ENSP00000307461.3; NM_015206.3; NP_056021.1.
DR UCSC; uc002bew.2; human.
DR CTD; 23251; -.
DR DisGeNET; 23251; -.
DR GeneCards; MINAR1; -.
DR HGNC; HGNC:29172; MINAR1.
DR HPA; ENSG00000169330; Tissue enhanced (adrenal gland, brain, retina).
DR MIM; 618054; gene.
DR neXtProt; NX_Q9UPX6; -.
DR OpenTargets; ENSG00000169330; -.
DR PharmGKB; PA162393036; -.
DR VEuPathDB; HostDB:ENSG00000169330; -.
DR eggNOG; ENOG502QSCS; Eukaryota.
DR GeneTree; ENSGT00530000063851; -.
DR HOGENOM; CLU_016692_0_0_1; -.
DR InParanoid; Q9UPX6; -.
DR OMA; IPDKRRV; -.
DR OrthoDB; 1321736at2759; -.
DR PhylomeDB; Q9UPX6; -.
DR TreeFam; TF350677; -.
DR PathwayCommons; Q9UPX6; -.
DR SignaLink; Q9UPX6; -.
DR BioGRID-ORCS; 23251; 9 hits in 1072 CRISPR screens.
DR GenomeRNAi; 23251; -.
DR Pharos; Q9UPX6; Tdark.
DR PRO; PR:Q9UPX6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UPX6; protein.
DR Bgee; ENSG00000169330; Expressed in right adrenal gland cortex and 114 other tissues.
DR ExpressionAtlas; Q9UPX6; baseline and differential.
DR Genevisible; Q9UPX6; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
DR InterPro; IPR039706; MINAR1-like.
DR InterPro; IPR009626; MINAR1-like_C.
DR PANTHER; PTHR31530; PTHR31530; 1.
DR Pfam; PF06789; MINAR1_C; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..916
FT /note="Major intrinsically disordered Notch2-binding
FT receptor 1"
FT /id="PRO_0000157133"
FT TOPO_DOM 1..891
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30080879"
FT TRANSMEM 892..912
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 913..916
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30080879"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3V7"
FT VARIANT 320
FT /note="V -> F (in dbSNP:rs11634652)"
FT /id="VAR_034044"
FT VARIANT 832
FT /note="I -> V (in dbSNP:rs2297773)"
FT /id="VAR_022042"
SQ SEQUENCE 916 AA; 102993 MW; 8A7831FA765197AF CRC64;
METSQETSLF LVKILEELDS KQNTVSYQDL CKSLCARFDL SQLAKLRSVL FYTACLDPNF
PATLFKDKMK CTVNNQQSKK IMVAADIVTI FNLIQMNGGA AKEKLPTGRQ KVRKKEASFE
SCRSDTEICN AAECEPLNCE LSERSFSRGY PIRQSSKCRK MDCKDCPQFV PASEPNFLLG
VSKEVKNRAA SLDRLQALAP YSVTSPQPCE MQRTYFPMNI ENESISDQDS LPINQSIKET
FISNEEPFVV QSCVQKRNIF KEDFHNLMAV SPSLVGPISK AENEHREPQS RKEPHKPPFF
NHSFEMPYNS QYLNPVYSPV PDKRRAKHES LDDLQASTYF GPTPVMGTQE ARRCLGKPNK
QTPWPAKSWS LNTEEVPDFE RSFFNRNPSE EKLHYPNASS QTPNFPAPER RPTYLVPKDQ
QPILPIAYAA KQNGLKSKEI SSPVDLEKHE PVKKFKDKSI NCTSGQLSSD TSSVGTQTEH
VLEPKKCRDL CTSGQGKYSD RHTMKHSDDD SEIVSDDISD IFRFLDDMSI SGSTGVIQSS
CYNSTGSLSQ LHKSDCDSSP EHNLTKIANG VPNSKGDKGN RPENTHHSEE ELKTSVCKLV
LRIGEIERKL ESLSGVRDEI SQVLGKLNKL DQKMQQPEKV SVQIDLNSLT SEGPSDDSAS
PRMFHAHSGS HGPKLENNPD WCCSDASGSN SESLRVKALK KSLFTRPSSR SLTEENSATE
SKIASISNSP RDWRTITYTN RVGLNEEEIK DTGPGDNKDW HRKSKEADRQ YDIPPQHRLP
KQPKDGFLVE QVFSPHPYPA SLKAHMKSNP LYTDMRLTEL AEVKRGQPSW TIEEYARNAG
DKGKLTALDL QTQESLNPNN LEYWMEDIYT PGYDSLLKRK EAEFRRAKVC KIAALIAAAA
CTVILVIVVP ICTMKS
